ID   ALGJ_AZOVI              Reviewed;         388 AA.
AC   O52197;
DT   25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   25-MAY-2022, entry version 62.
DE   RecName: Full=Probable alginate O-acetylase AlgJ;
DE            EC=2.3.1.-;
DE   AltName: Full=Alginate biosynthesis protein AlgJ;
DE   Flags: Precursor;
GN   Name=algJ; Synonyms=algV;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 9046;
RX   PubMed=10352233; DOI=10.1016/s0378-1119(99)00119-5;
RA   Vazquez-Ramos A., Moreno S., Guzman J., Alvarado A., Espin G.;
RT   "Transcriptional organization of the Azotobacter vinelandii algGXLVIFA
RT   genes: characterization of algF mutants.";
RL   Gene 232:217-222(1999).
CC   -!- FUNCTION: Together with AlgI and AlgF, forms an inner membrane complex
CC       which probably interacts with the alginate polymerization-transport
CC       complex and adds acetyl groups at the O-2 and O-3 positions of
CC       mannuronate residues. Acetylation of alginate increases cyst resistance
CC       to desiccation.
CC   -!- PATHWAY: Glycan biosynthesis; alginate biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Peripheral
CC       membrane protein {ECO:0000250}; Periplasmic side {ECO:0000250}.
CC       Periplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AlgJ family. {ECO:0000305}.
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DR   EMBL; AF027499; AAC04569.1; -; Genomic_DNA.
DR   RefSeq; WP_012699740.1; NZ_FPKM01000036.1.
DR   AlphaFoldDB; O52197; -.
DR   SMR; O52197; -.
DR   OMA; FNEGRPG; -.
DR   UniPathway; UPA00286; -.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd14442; AlgJ_like; 1.
DR   InterPro; IPR034657; AlgJ.
DR   InterPro; IPR031811; ALGX/ALGJ_SGNH-like.
DR   Pfam; PF16822; ALGX; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Alginate biosynthesis; Cell inner membrane; Cell membrane;
KW   Membrane; Periplasm; Signal; Transferase.
FT   SIGNAL          1..29
FT                   /evidence="ECO:0000255"
FT   CHAIN           30..388
FT                   /note="Probable alginate O-acetylase AlgJ"
FT                   /id="PRO_0000001119"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        192
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        288
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   388 AA;  42499 MW;  F45A1336A7CFCC96 CRC64;
     MNRTTNLVYA GTFAGTLLAL SLWSLKGAAG FSTADNTPVL NGKLALAFEK HYDEEFPIKK
     LGTNLWAALD YTLFGEGRPG VVIGANQWLF SDEEFKPTAA ASQNITDNQA LIQGVRETLA
     RNNVQLVMAI LPAKARLYPE NFGEQQPASL HEQLYQNFRR IVADAGIQAP DLLGPLQQAK
     AGGQVFLRTD THWTPYGAQV VAGQLATTIK PIGVLPESGN VYVTETLPGG PHKGDLTNFL
     PLDPLFEELL PPPDQLAKHN TRQQEESAPA GDDLFAETQV PVALVGTSYS ADERWNFAGA
     LRQALGSDLV NFAEDGRGPL LPMLKFLQSE DFKKSPPRLV IWEFPERYLP MAYDLSEFDA
     DWIAQLKAAG RQDKQLADNT ATNQGARH